1h1a: Difference between revisions

The crystal structures of thermophilic xylanases from Chaetomium, thermophilum and Nonomuraea flexuosa were determined at 1.75 and 2.1 A, resolution, respectively. Both enzymes have the overall fold typical to, family 11 xylanases with two highly twisted beta-sheets forming a large, cleft. The comparison of 12 crystal structures of family 11 xylanases from, both mesophilic and thermophilic organisms showed that the structures of, different xylanases are very similar. The sequence identity differences, correlated well with the structural differences. Several minor, modifications appeared to be responsible for the increased thermal, stability of family 11 xylanases: (a) higher Thr : Ser ratio (b) increased, number of charged residues, especially Arg, resulting in enhanced polar, interactions, and (c) improved stabilization of secondary structures, involved the higher number of residues in the beta-strands and, stabilization of the alpha-helix region. Some members of family 11, xylanases have a unique strategy to improve their stability, such as a, higher number of ion pairs or aromatic residues on protein surface, a more, compact structure, a tighter packing, and insertions at some regions, resulting in enhanced interactions.

1H1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum] with SO4, CA, S and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Structure known Active Site: S1A. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H1A OCA].  

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